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1e31
From Proteopedia
| 1e31, resolution 2.71Å () | |||||||||
|---|---|---|---|---|---|---|---|---|---|
| Ligands: | , | ||||||||
| Domains: | BIR | ||||||||
| |||||||||
| Resources: | FirstGlance, OCA, PDBsum, RCSB | ||||||||
| Coordinates: | save as pdb, mmCIF, xml | ||||||||
SURVIVIN DIMER H. SAPIENS
Survivin is a mitotic spindle-associated protein involved in linking mitotic spindle function to activation of apoptosis in mammalian cells. The structure of the full-length human survivin has been determined by X-ray crystallography to 2.7 A. Strikingly, the structure forms a very unusual bow tie-shaped dimer. It does not dimerize through a C-terminal coiled-coil, contrary to sequence analysis prediction. The C-terminal helices contain hydrophobic clusters with the potential for protein-protein interactions. The unusual shape and dimensions of survivin suggest it serves an adaptor function through its alpha-helical extensions.
Crystal structure of human survivin reveals a bow tie-shaped dimer with two unusual alpha-helical extensions., Chantalat L, Skoufias DA, Kleman JP, Jung B, Dideberg O, Margolis RL, Mol Cell. 2000 Jul;6(1):183-9. PMID:10949039
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
About this Structure
1E31 is a 2 chains structure of sequences from Homo sapiens. Full crystallographic information is available from OCA.
Reference
- Chantalat L, Skoufias DA, Kleman JP, Jung B, Dideberg O, Margolis RL. Crystal structure of human survivin reveals a bow tie-shaped dimer with two unusual alpha-helical extensions. Mol Cell. 2000 Jul;6(1):183-9. PMID:10949039
Page seeded by OCA on Tue Feb 17 08:19:18 2009
